Inhibition of bovine brain aldehyde reductase by anticonvulsant compounds in vitro
Identifieur interne : 000E16 ( Main/Merge ); précédent : 000E15; suivant : 000E17Inhibition of bovine brain aldehyde reductase by anticonvulsant compounds in vitro
Auteurs : V. Gene Erwin ; Richard A. Deitrich [États-Unis]Source :
- Biochemical Pharmacology [ 0006-2952 ] ; 1973.
English descriptors
- Teeft :
- Aldehyde, Aldehyde reductase, Aldehyde reductase activity, Anticonvulsant, Anticonvulsant actions, Anticonvulsant activity, Anticonvulsant compounds, Assay system, Barbiturate, Bovine, Bovine brain aldehyde reductase, Bovine brain aldehyde reductase inhibition, Brain aldehyde reductase activity, Brain tissue, Derivative, Dimethadione, Diphenylhydantoin, Enzyme activity, Enzyme protein, Erwin, Ethosuximide, Ethotoin, Experimental conditions, Hydantoin, Inhibition, Inhibitor, Nadph, Nadph oxidation, Nmoles nadph, Noncompetitive, Pharmac, Phenobarbital, Reaction mixture, Reaction mixtures, Reductase, Sodium phosphate, Specific activity, Trimethadione, Variable substrate, Various anticonvulsants, Various barbiturates, Various compounds, Various inhibitors.
Abstract
Abstract: The catalytic activity of partially purified NADPH-linked aldehyde reductase (alcohol: NADP oxidoreductase, EC 1.1.1.2) from bovine brain was markedly inhibited in vitro by anticonvulsant compounds. In general, the ability of these drugs to inhibit aldehyde reductase in vitro paralleled their anticonvulsant activity. Inhibition by various barbiturates, hydantoins or succinimides was non-competitive with either NADPH or aldehyde as the variable substrate, whereas the 2,4-oxazolidinediones produced a mixed type of inhibition. Inhibition by all ionizable compounds was found to vary with the pH of the reaction mixture, while the non-ionizable substances, paradione, trimethadione, methsuximide, 3-methyl-5-ethyl-5-phenylhydantoin, were not inhibitory. At pH 7.0 the inhibitor constants (Ki values) for phenobarbital, 5,5-diphenylhydantoin, 5,5-dimethyloxazolidinedione and ethosuximide were 1.2 × 10−4 M, 1.7 × 10−4 M, 4.7 × 10−4 M and 5.5 × 10−3 M respectively. The possibility that inhibition of brain NADPH-linked aldehyde reductase by these agents is concerned with their anticonvulsant actions is discussed.
Url:
DOI: 10.1016/0006-2952(73)90070-1
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Gene Erwin</name></author><author><name sortKey="Deitrich, Richard A" sort="Deitrich, Richard A" uniqKey="Deitrich R" first="Richard A." last="Deitrich">Richard A. Deitrich</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>School of Pharmacy, University of Colorado, Boulder, Col. 80302</wicri:regionArea><wicri:noRegion>Col. 80302</wicri:noRegion></affiliation><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pharmacology, University of Colorado Medical Center, Denver, Col. 80220</wicri:regionArea><wicri:noRegion>Col. 80220</wicri:noRegion></affiliation><affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Biochemical Pharmacology</title><title level="j" type="abbrev">BCP</title><idno type="ISSN">0006-2952</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1973">1973</date><biblScope unit="volume">22</biblScope><biblScope unit="issue">20</biblScope><biblScope unit="page" from="2615">2615</biblScope><biblScope unit="page" to="2624">2624</biblScope></imprint><idno type="ISSN">0006-2952</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0006-2952</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Aldehyde</term><term>Aldehyde reductase</term><term>Aldehyde reductase activity</term><term>Anticonvulsant</term><term>Anticonvulsant actions</term><term>Anticonvulsant activity</term><term>Anticonvulsant compounds</term><term>Assay system</term><term>Barbiturate</term><term>Bovine</term><term>Bovine brain aldehyde reductase</term><term>Bovine brain aldehyde reductase inhibition</term><term>Brain aldehyde reductase activity</term><term>Brain tissue</term><term>Derivative</term><term>Dimethadione</term><term>Diphenylhydantoin</term><term>Enzyme activity</term><term>Enzyme protein</term><term>Erwin</term><term>Ethosuximide</term><term>Ethotoin</term><term>Experimental conditions</term><term>Hydantoin</term><term>Inhibition</term><term>Inhibitor</term><term>Nadph</term><term>Nadph oxidation</term><term>Nmoles nadph</term><term>Noncompetitive</term><term>Pharmac</term><term>Phenobarbital</term><term>Reaction mixture</term><term>Reaction mixtures</term><term>Reductase</term><term>Sodium phosphate</term><term>Specific activity</term><term>Trimethadione</term><term>Variable substrate</term><term>Various anticonvulsants</term><term>Various barbiturates</term><term>Various compounds</term><term>Various inhibitors</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The catalytic activity of partially purified NADPH-linked aldehyde reductase (alcohol: NADP oxidoreductase, EC 1.1.1.2) from bovine brain was markedly inhibited in vitro by anticonvulsant compounds. In general, the ability of these drugs to inhibit aldehyde reductase in vitro paralleled their anticonvulsant activity. Inhibition by various barbiturates, hydantoins or succinimides was non-competitive with either NADPH or aldehyde as the variable substrate, whereas the 2,4-oxazolidinediones produced a mixed type of inhibition. Inhibition by all ionizable compounds was found to vary with the pH of the reaction mixture, while the non-ionizable substances, paradione, trimethadione, methsuximide, 3-methyl-5-ethyl-5-phenylhydantoin, were not inhibitory. At pH 7.0 the inhibitor constants (Ki values) for phenobarbital, 5,5-diphenylhydantoin, 5,5-dimethyloxazolidinedione and ethosuximide were 1.2 × 10−4 M, 1.7 × 10−4 M, 4.7 × 10−4 M and 5.5 × 10−3 M respectively. The possibility that inhibition of brain NADPH-linked aldehyde reductase by these agents is concerned with their anticonvulsant actions is discussed.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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